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首页> 外文期刊>Biotechnology Progress >Antioxidant Efficacy and Adhesion Rescue by a Recombinant Mussel Foot Protein-6
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Antioxidant Efficacy and Adhesion Rescue by a Recombinant Mussel Foot Protein-6

机译：重组贻贝足蛋白6的抗氧化功效和黏附救援。

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摘要

Mytilus foot protein type 6 (mfp-6) is crucial for maintaining the reducing conditions needed for optimal wet adhesion in marine mussels. In this report, we describe the expression and production of a recombinant Mytilus californianus foot protein type 6 variant 1 (rmfp-6.1) fused with a hexahistidine affinity tag in Escherichia coli and its purification by affinity chromatography. Recombinant mfp-6 showed high purification yields of 5-6 mg L~(-1) cell culture and excellent solubility in low pH buffers that retard oxidation of its many thiol groups. Purified rmfp-6.1 protein showed high 2,2-diphenyl-l-picrylhydrazyl radical scavenging activity when compared with vitamin C. Using the highly sensitive surface forces apparatus (SFA) technique to measure interfacial surface forces in the nano-Newton range, we show that rmfp-6.1 is also able to rescue the oxidation-dependent adhesion loss of mussel foot protein 3 (mfp-3) at pH 3. The adhesion rescue is related to a reduction of dopaquinone back to 3,4-dihydroxyphenyl-L-alanine in mfp-3, which is the reverse reaction observed during the detrimental enzymatic browning process in fruits and vegetables. Broadly viewed, rmfp-6.1 has potential as a versatile antioxidant for applications ranging from personal products to antispoilants for perishable foods during processing and storage.
机译：6型Mytilus足蛋白（mfp-6）对于维持海洋贻贝最佳湿润粘附所需的还原条件至关重要。在此报告中，我们描述了在大肠杆菌中融合了六组氨酸亲和标签的重组Mytilus californianus脚6型变体1（rmfp-6.1）的表达和生产，并通过亲和色谱法进行了纯化。重组mfp-6表现出5-6 mg L〜（-1）细胞培养物的高纯化产率，并且在低pH缓冲液中具有出色的溶解性，从而阻碍了其许多巯基的氧化。与维生素C相比，纯化的rmfp-6.1蛋白显示出较高的2,2-二苯基-1-吡咯并肼基自由基清除活性。使用高灵敏度表面力仪器（SFA）技术测量纳米牛顿范围内的界面表面力rmfp-6.1还能在pH 3的情况下挽救贻贝足蛋白3（mfp-3）的氧化依赖性黏附损失。黏附挽救与多巴醌还原为3,4-二羟基苯基-L-丙氨酸有关在mfp-3中，这是有害的水果和蔬菜酶促褐变过程中观察到的逆反应。广为人知，rmfp-6.1具有作为多功能抗氧化剂的潜力，可用于从个人产品到加工和储存过程中易腐烂食品的防腐败剂。

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